Enzyme

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     2. Transferases
        2.6 Transferring nitrogenous groups
            2.6.1 Transaminases
ID:2.6.1.7
Description:Kynurenine--oxoglutarate transaminase.
Alternative Name: Kynurenine--oxoglutarate aminotransferase.
Kynurenine aminotransferase.
Cath: 3.40.640.10; 3.90.1150.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.6.1.7
BRENDA Enzyme Link: BRENDA 2.6.1.7
KEGG Enzyme Link: KEGG2.6.1.7
BioCyc Enzyme Link: BioCyc 2.6.1.7
ExPASy Enzyme Link: ExPASy2.6.1.7
EC2PDB Enzyme Link: EC2PDB 2.6.1.7
ExplorEnz Enzyme Link: ExplorEnz 2.6.1.7
PRIAM enzyme-specific profiles Link: PRIAM 2.6.1.7
IntEnz Enzyme Link: IntEnz 2.6.1.7
MEDLINE Enzyme Link: MEDLINE 2.6.1.7
MSA:

2.6.1.7;

Phylogenetic Tree:

2.6.1.7;

Uniprot:
M-CSA:
RHEA:20964 2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[*:7])-[NH2;+0:8]>>[*:5]-[C;H0;+0:6](-[*:7])=[O;H0;+0:4].[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:8]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of human kynurenine aminotransferase I.Rossi F, Han Q, Li J, Li J, Rizzi M2004 Nov 2615364907